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Etude fonctionnelle du dégradosome d'Escherichia coli et régulation de la RNase E par phosphorylation

Isabelle Toesca
Abstract : The RNA degradosome of E. coli is a multienzymatic complex involved in mRNA degradation. It is composed of four major proteins: RNase E, PNPase, RhlB and enolase. In our first study, we examined the interaction between RNase E and RhlB, and other DEAD-box RNA helicases. We showed the existence of two distinct helicase binding sites: one that is RhlB specific and another that binds SrmB, RhlE or CsdA. A second study was aimed at elucidating the role of enolase in the degadosome. Considering these results, the hypothesis that enolase has a general role in mRNA degradation seems unlikely. Studies on inhibition of the RNase E due to phosphorylation of its non-catalytic domain by a protein kinase from bacteriophage T7 led to mechanistic models for the control of RNase E activity. In addition, these studies showed a close link between the catalytic and non-catalytic domains of RNase E. Furthermore, there apparently is an endogenous kinase in E. coli that phosphorylates the non-catalytic domain of the RNase E, but only in the absence of the catalytic domain.
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https://tel.archives-ouvertes.fr/tel-00010049
Contributor : Chantal Michel <>
Submitted on : Tuesday, September 6, 2005 - 2:20:53 PM
Last modification on : Tuesday, September 6, 2005 - 2:20:53 PM
Long-term archiving on: : Friday, April 2, 2010 - 10:18:01 PM

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  • HAL Id : tel-00010049, version 1

Citation

Isabelle Toesca. Etude fonctionnelle du dégradosome d'Escherichia coli et régulation de la RNase E par phosphorylation. Biochimie [q-bio.BM]. Université Paul Sabatier - Toulouse III, 2005. Français. ⟨tel-00010049⟩

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